VPS34 Recombinant Rabbit mAb

VPS34, also known as PIK3C3, is the sole class III phosphatidylinositol 3-kinase in mammals and plays a central role in intracellular membrane trafficking, autophagy, and signal transduction. Its structure consists of an N-terminal C2 domain, a central PIK helical domain, and a C-terminal kinase catalytic domain, with the kinase domain specifically responsible for catalyzing the conversion of phosphatidylinositol (PtdIns) to phosphatidylinositol 3-phosphate (PI3P). It exerts its functions by forming distinct complexes with different regulatory subunits—such as VPS15 and Beclin 1—and their interaction partners: the complex I formed with ATG14 primarily regulates autophagosome formation, whereas the complex II formed with UVRAG mainly regulates endocytic trafficking and vesicular transport. The generated PI3P signaling molecule specifically recruits effector proteins containing FYVE or PX domains, thereby orchestrating key steps such as vesicle docking, membrane fusion, and endosomal sorting. Through these functions, VPS34 integrates nutrient sensing, cellular stress responses, and intracellular transport, making it essential for maintaining cellular homeostasis. Notably, dysregulation of VPS34 function has been linked to various pathological processes, including tumorigenesis and cardiovascular diseases.